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- W2018761162 abstract "In the presence of ATP, Mg2+ and CoA, mouse brain synaptosomes actively catalyze the transfer of arachidonate to 1-acyl-phosphoglycerides. The enzymic acylation process was inhibited greatly by 0.1 mm-PCMB (parachloromercuric benzoate), and only partially by 0.1 mm-DNP (2,4-dini-trophenol) and 0.001% (w/v) oligomycin. Arachidonoyl transfer to 1-acyl-glycerophosphorylcholines and 1-acyl-glycerophosphorylinositols was negligibly affected by 1 mm-NaF and 10 mm-glucose. Among the different 1-acyl-phosphoglycerides used as acceptor molecules, the relative order for arachidonoyl transfer activity was: 1-acyl-glycerophosphorylinositols > 1-acyl-glycerophosphorylcholines > l-acyl-glycerophosphorylethanolamines. The ester linkage at the C-1 position of the 1-acyl-phosphoglycerides also appears necessary for activity for no arachidonoyl transfer activity was observed when 1-alkenyl-glycerophosphorylethanolamines were used as the acceptor molecules. Arachidonate transfer to 1-acyl-glycerophosphorylinositols was optimal at low acceptor concentrations (10–30 μm) whereas the transfer to 1-acyl-glycerophosphorylcholines occurred over a much broader range of acceptor concentrations (30–80 μm). At optimal acceptor concentration, maximal transfer activity was observed at arachidonate concentration of 50–80 μm. The newly synthesized phosphoglycerides were found distributed in the subsynaptic components with specific activity highest in the fraction containing synaptic vesicles." @default.
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- W2018761162 date "1978-01-01" @default.
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- W2018761162 title "CHARACTERIZATION OF THE ENZYMIC TRANSFER OF ARACHIDONOYL GROUPS TO 1-ACYL-PHOSPHOGLYCERIDES IN MOUSE SYNAPTOSOME FRACTION" @default.
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- W2018761162 doi "https://doi.org/10.1111/j.1471-4159.1978.tb07037.x" @default.
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